ID   DEOC_COCIM              Reviewed;         267 AA.
AC   P0CH94; J3KH18; J3KH34;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Deoxyribose-phosphate aldolase;
DE            Short=DERA;
DE            EC=4.1.2.4;
DE   AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase;
DE   AltName: Full=Phosphodeoxyriboaldolase;
DE            Short=Deoxyriboaldolase;
GN   ORFNames=CIMG_00461;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
CC   -!- FUNCTION: Catalyzes a reversible aldol reaction between acetaldehyde
CC       and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-
CC       phosphate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde
CC         3-phosphate; Xref=Rhea:RHEA:12821, ChEBI:CHEBI:15343,
CC         ChEBI:CHEBI:59776, ChEBI:CHEBI:62877; EC=4.1.2.4;
CC   -!- PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate
CC       degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-
CC       deoxy-alpha-D-ribose 1-phosphate: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; GG704911; EAS35107.3; -; Genomic_DNA.
DR   RefSeq; XP_001246690.1; XM_001246689.2.
DR   AlphaFoldDB; P0CH94; -.
DR   SMR; P0CH94; -.
DR   STRING; 246410.P0CH94; -.
DR   EnsemblFungi; EAS35107; EAS35107; CIMG_00461.
DR   GeneID; 4566357; -.
DR   KEGG; cim:CIMG_00461; -.
DR   VEuPathDB; FungiDB:CIMG_00461; -.
DR   InParanoid; P0CH94; -.
DR   OMA; MNACIPP; -.
DR   OrthoDB; 1349979at2759; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR   GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00959; DeoC; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00114; DeoC_type1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011343; DeoC.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR028581; DeoC_typeI.
DR   PANTHER; PTHR10889; PTHR10889; 1.
DR   PANTHER; PTHR10889:SF1; PTHR10889:SF1; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF001357; DeoC; 1.
DR   SMART; SM01133; DeoC; 1.
DR   TIGRFAMs; TIGR00126; deoC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lyase; Reference proteome; Schiff base.
FT   CHAIN           1..267
FT                   /note="Deoxyribose-phosphate aldolase"
FT                   /id="PRO_0000398843"
FT   ACT_SITE        123
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L0"
FT   ACT_SITE        185
FT                   /note="Schiff-base intermediate with acetaldehyde"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L0"
FT   ACT_SITE        217
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L0"
SQ   SEQUENCE   267 AA;  28872 MW;  E05A0AE1F723F869 CRC64;
     MSSLNNEEWD LLISGKKATL QYPIPLLCYP APEVVSIAQI IDHTQLSLSA TGSQIDVLCA
     EAKEYGFATV CVRPDYVSRA VQYLQGTQVG VTCVIGFHEG TYSTDQKVSE AKRAMQNGAS
     ELDMVMNYPW LSEKRYTDVF QDIRAVRLAA KDAILKVILE TSQLTADEII AGCVLSSLAG
     ADYVKTSTGF NGPGASIENV SLMSAVCDSL QSETRVKASG GIRTIEDCVK MVRAGAERLG
     ASAGVKIVNE TRLGNRQVDE PMEPTNY